Carroll A G, Wagner P D
Laboratory of Biochemistry, National Cancer Institute, Bethesda, MD 20982.
J Muscle Res Cell Motil. 1989 Oct;10(5):379-84. doi: 10.1007/BF01758434.
We have examined the effect of protein kinase C phosphorylation on the actin-activated ATPase activity and filament stability of calf thymus myosin. Protein kinase C phosphorylated thymus myosin regulatory light chains, LC20, on two sites which are different from the site phosphorylated by myosin light chain kinase. The light meromyosin part of the thymus myosin heavy chain was also phosphorylated by protein kinase C, but at a rate about 10% that of LC20. Under conditions where both unphosphorylated thymus and myosin light chain kinase-phosphorylated thymus myosin were filamentous and under conditions where myosin light chain kinase phosphorylation induces myosin filament formation, protein kinase C phosphorylation had little effect on the actin-activated ATPase activity or filament stability of unphosphorylated or myosin light chain kinase-phosphorylated myosin. In contrast, protein kinase C phosphorylation has been reported to inhibit the actin-activated ATPase activity of gizzard myosin.
